HEADER TRANSFERASE, LYASE 01-APR-03 1OX6
TITLE TOWARDS UNDERSTANDING THE MECHANISM OF THE COMPLEX CYCLIZATION
TITLE 2 REACTION CATALYZED BY IMIDAZOLE GLYCEROPHOSPHATE SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE HISHF;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: AMIDOTRANSFERASE AND CYCLASE DOMAINS;
COMPND 5 SYNONYM: HISTIDINE BIOSYNTHESIS BIFUNCTIONAL AMIDOTRANSFERASE; IGP
COMPND 6 SYNTHASE; IMGP SYNTHASE; IGPS; GLUTAMINE AMIDOTRANSFERASE:CYCLASE;
COMPND 7 EC: 2.4.2.-, 4.1.3.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: HIS7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COMPLEX CYCLIZATION; IMIDAZOLE GLYCEROPHOSPHATE SYNTHASE,
KEYWDS 2 TRANSFERASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.N.CHAUDHURI,J.L.SMITH
REVDAT 3 16-AUG-23 1OX6 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1OX6 1 VERSN
REVDAT 1 17-JUN-03 1OX6 0
JRNL AUTH B.N.CHAUDHURI,S.C.LANGE,R.S.MYERS,V.J.DAVISSON,J.L.SMITH
JRNL TITL TOWARDS UNDERSTANDING THE MECHANISM OF THE COMPLEX
JRNL TITL 2 CYCLIZATION REACTION CATALYZED BY IMIDAZOLE GLYCEROPHOSPHATE
JRNL TITL 3 SYNTHASE: CRYSTAL STRUCTURES OF A TERNARY COMPLEX AND THE
JRNL TITL 4 FREE ENZYME
JRNL REF BIOCHEMISTRY V. 42 7003 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12795595
JRNL DOI 10.1021/BI034320H
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.S.MYERS,J.R.JENSEN,I.L.DERAS,J.L.SMITH,V.J.DAVISSON
REMARK 1 TITL SUBSTRATE-INDUCED CHANGES IN THE AMMONIA CHANNEL FOR
REMARK 1 TITL 2 IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE
REMARK 1 REF BIOCHEMISTRY V. 42 7013 2003
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI034314L
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1517144.100
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 44.7000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 46100
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2317
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7240
REMARK 3 BIN R VALUE (WORKING SET) : 0.2790
REMARK 3 BIN FREE R VALUE : 0.3210
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 373
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8256
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 281
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.00000
REMARK 3 B22 (A**2) : -9.66000
REMARK 3 B33 (A**2) : 0.66000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.28
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.37
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.350
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.870
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.340 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.240 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.930 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.930 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 29.29
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DISORDERED REGIONS WERE MODELED
REMARK 3 STEREOCHEMICALLY
REMARK 4
REMARK 4 1OX6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018763.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAR-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03320
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-2
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47205
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : 0.10600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1JVN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PEG MME 5000, MES,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 48.50000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.40000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.40000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.50000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 THR A 257
REMARK 465 LYS A 258
REMARK 465 GLY A 259
REMARK 465 ASP A 260
REMARK 465 GLN A 261
REMARK 465 TYR A 262
REMARK 465 ASP A 263
REMARK 465 VAL A 264
REMARK 465 ARG A 265
REMARK 465 GLU A 266
REMARK 465 LYS A 267
REMARK 465 SER A 268
REMARK 465 ASP A 269
REMARK 465 GLY A 270
REMARK 465 LYS A 271
REMARK 465 GLY A 272
REMARK 465 VAL A 273
REMARK 465 ARG A 274
REMARK 465 ASN A 275
REMARK 465 SER A 301
REMARK 465 PHE A 302
REMARK 465 ARG A 303
REMARK 465 GLU A 551
REMARK 465 GLU A 552
REMARK 465 THR B 257
REMARK 465 LYS B 258
REMARK 465 GLY B 259
REMARK 465 ASP B 260
REMARK 465 GLN B 261
REMARK 465 TYR B 262
REMARK 465 ASP B 263
REMARK 465 VAL B 264
REMARK 465 ARG B 265
REMARK 465 GLU B 266
REMARK 465 LYS B 267
REMARK 465 SER B 268
REMARK 465 ASP B 269
REMARK 465 GLY B 270
REMARK 465 LYS B 271
REMARK 465 GLY B 272
REMARK 465 VAL B 273
REMARK 465 ARG B 274
REMARK 465 ASN B 275
REMARK 465 SER B 301
REMARK 465 PHE B 302
REMARK 465 ARG B 303
REMARK 465 GLU B 551
REMARK 465 GLU B 552
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A -2 7.05 -165.59
REMARK 500 CYS A 83 -110.44 55.44
REMARK 500 PRO A 97 -37.90 -37.35
REMARK 500 ASP A 106 32.07 -75.57
REMARK 500 ASN A 185 -118.19 49.00
REMARK 500 PRO A 217 154.49 -48.83
REMARK 500 TYR A 234 7.23 58.96
REMARK 500 ILE A 299 67.69 -114.26
REMARK 500 PHE A 324 53.30 -98.57
REMARK 500 GLN A 413 -19.27 -49.96
REMARK 500 SER A 500 117.89 83.80
REMARK 500 ALA A 523 -92.32 -123.83
REMARK 500 SER B -2 11.97 -174.60
REMARK 500 CYS B 83 -111.83 58.17
REMARK 500 PRO B 97 -37.10 -37.97
REMARK 500 ASN B 185 -117.18 50.06
REMARK 500 PRO B 217 154.01 -47.20
REMARK 500 TYR B 234 8.94 57.84
REMARK 500 ASN B 249 -165.54 -79.07
REMARK 500 ILE B 299 67.53 -115.68
REMARK 500 PHE B 324 52.60 -98.66
REMARK 500 SER B 500 118.22 81.85
REMARK 500 ALA B 523 -93.29 -124.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 902 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A -3 N
REMARK 620 2 SER A -2 N 75.4
REMARK 620 3 HIS A -1 ND1 106.3 176.3
REMARK 620 4 HIS A -1 N 153.5 78.3 100.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 901 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B -3 N
REMARK 620 2 SER B -2 N 79.5
REMARK 620 3 HIS B -1 ND1 101.3 172.6
REMARK 620 4 HIS B -1 N 161.2 81.9 97.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POP B 999
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JVN RELATED DB: PDB
REMARK 900 RELATED ID: 1OX4 RELATED DB: PDB
REMARK 900 RELATED ID: 1OX5 RELATED DB: PDB
DBREF 1OX6 A 1 552 UNP P33734 HIS5_YEAST 1 552
DBREF 1OX6 B 1 552 UNP P33734 HIS5_YEAST 1 552
SEQADV 1OX6 GLY A -3 UNP P33734 CLONING ARTIFACT
SEQADV 1OX6 SER A -2 UNP P33734 CLONING ARTIFACT
SEQADV 1OX6 HIS A -1 UNP P33734 CLONING ARTIFACT
SEQADV 1OX6 GLY B -3 UNP P33734 CLONING ARTIFACT
SEQADV 1OX6 SER B -2 UNP P33734 CLONING ARTIFACT
SEQADV 1OX6 HIS B -1 UNP P33734 CLONING ARTIFACT
SEQRES 1 A 555 GLY SER HIS MET PRO VAL VAL HIS VAL ILE ASP VAL GLU
SEQRES 2 A 555 SER GLY ASN LEU GLN SER LEU THR ASN ALA ILE GLU HIS
SEQRES 3 A 555 LEU GLY TYR GLU VAL GLN LEU VAL LYS SER PRO LYS ASP
SEQRES 4 A 555 PHE ASN ILE SER GLY THR SER ARG LEU ILE LEU PRO GLY
SEQRES 5 A 555 VAL GLY ASN TYR GLY HIS PHE VAL ASP ASN LEU PHE ASN
SEQRES 6 A 555 ARG GLY PHE GLU LYS PRO ILE ARG GLU TYR ILE GLU SER
SEQRES 7 A 555 GLY LYS PRO ILE MET GLY ILE CYS VAL GLY LEU GLN ALA
SEQRES 8 A 555 LEU PHE ALA GLY SER VAL GLU SER PRO LYS SER THR GLY
SEQRES 9 A 555 LEU ASN TYR ILE ASP PHE LYS LEU SER ARG PHE ASP ASP
SEQRES 10 A 555 SER GLU LYS PRO VAL PRO GLU ILE GLY TRP ASN SER CYS
SEQRES 11 A 555 ILE PRO SER GLU ASN LEU PHE PHE GLY LEU ASP PRO TYR
SEQRES 12 A 555 LYS ARG TYR TYR PHE VAL HIS SER PHE ALA ALA ILE LEU
SEQRES 13 A 555 ASN SER GLU LYS LYS LYS ASN LEU GLU ASN ASP GLY TRP
SEQRES 14 A 555 LYS ILE ALA LYS ALA LYS TYR GLY SER GLU GLU PHE ILE
SEQRES 15 A 555 ALA ALA VAL ASN LYS ASN ASN ILE PHE ALA THR GLN PHE
SEQRES 16 A 555 HIS PRO GLU LYS SER GLY LYS ALA GLY LEU ASN VAL ILE
SEQRES 17 A 555 GLU ASN PHE LEU LYS GLN GLN SER PRO PRO ILE PRO ASN
SEQRES 18 A 555 TYR SER ALA GLU GLU LYS GLU LEU LEU MET ASN ASP TYR
SEQRES 19 A 555 SER ASN TYR GLY LEU THR ARG ARG ILE ILE ALA CYS LEU
SEQRES 20 A 555 ASP VAL ARG THR ASN ASP GLN GLY ASP LEU VAL VAL THR
SEQRES 21 A 555 LYS GLY ASP GLN TYR ASP VAL ARG GLU LYS SER ASP GLY
SEQRES 22 A 555 LYS GLY VAL ARG ASN LEU GLY LYS PRO VAL GLN LEU ALA
SEQRES 23 A 555 GLN LYS TYR TYR GLN GLN GLY ALA ASP GLU VAL THR PHE
SEQRES 24 A 555 LEU ASN ILE THR SER PHE ARG ASP CYS PRO LEU LYS ASP
SEQRES 25 A 555 THR PRO MET LEU GLU VAL LEU LYS GLN ALA ALA LYS THR
SEQRES 26 A 555 VAL PHE VAL PRO LEU THR VAL GLY GLY GLY ILE LYS ASP
SEQRES 27 A 555 ILE VAL ASP VAL ASP GLY THR LYS ILE PRO ALA LEU GLU
SEQRES 28 A 555 VAL ALA SER LEU TYR PHE ARG SER GLY ALA ASP LYS VAL
SEQRES 29 A 555 SER ILE GLY THR ASP ALA VAL TYR ALA ALA GLU LYS TYR
SEQRES 30 A 555 TYR GLU LEU GLY ASN ARG GLY ASP GLY THR SER PRO ILE
SEQRES 31 A 555 GLU THR ILE SER LYS ALA TYR GLY ALA GLN ALA VAL VAL
SEQRES 32 A 555 ILE SER VAL ASP PRO LYS ARG VAL TYR VAL ASN SER GLN
SEQRES 33 A 555 ALA ASP THR LYS ASN LYS VAL PHE GLU THR GLU TYR PRO
SEQRES 34 A 555 GLY PRO ASN GLY GLU LYS TYR CYS TRP TYR GLN CYS THR
SEQRES 35 A 555 ILE LYS GLY GLY ARG GLU SER ARG ASP LEU GLY VAL TRP
SEQRES 36 A 555 GLU LEU THR ARG ALA CYS GLU ALA LEU GLY ALA GLY GLU
SEQRES 37 A 555 ILE LEU LEU ASN CYS ILE ASP LYS ASP GLY SER ASN SER
SEQRES 38 A 555 GLY TYR ASP LEU GLU LEU ILE GLU HIS VAL LYS ASP ALA
SEQRES 39 A 555 VAL LYS ILE PRO VAL ILE ALA SER SER GLY ALA GLY VAL
SEQRES 40 A 555 PRO GLU HIS PHE GLU GLU ALA PHE LEU LYS THR ARG ALA
SEQRES 41 A 555 ASP ALA CYS LEU GLY ALA GLY MET PHE HIS ARG GLY GLU
SEQRES 42 A 555 PHE THR VAL ASN ASP VAL LYS GLU TYR LEU LEU GLU HIS
SEQRES 43 A 555 GLY LEU LYS VAL ARG MET ASP GLU GLU
SEQRES 1 B 555 GLY SER HIS MET PRO VAL VAL HIS VAL ILE ASP VAL GLU
SEQRES 2 B 555 SER GLY ASN LEU GLN SER LEU THR ASN ALA ILE GLU HIS
SEQRES 3 B 555 LEU GLY TYR GLU VAL GLN LEU VAL LYS SER PRO LYS ASP
SEQRES 4 B 555 PHE ASN ILE SER GLY THR SER ARG LEU ILE LEU PRO GLY
SEQRES 5 B 555 VAL GLY ASN TYR GLY HIS PHE VAL ASP ASN LEU PHE ASN
SEQRES 6 B 555 ARG GLY PHE GLU LYS PRO ILE ARG GLU TYR ILE GLU SER
SEQRES 7 B 555 GLY LYS PRO ILE MET GLY ILE CYS VAL GLY LEU GLN ALA
SEQRES 8 B 555 LEU PHE ALA GLY SER VAL GLU SER PRO LYS SER THR GLY
SEQRES 9 B 555 LEU ASN TYR ILE ASP PHE LYS LEU SER ARG PHE ASP ASP
SEQRES 10 B 555 SER GLU LYS PRO VAL PRO GLU ILE GLY TRP ASN SER CYS
SEQRES 11 B 555 ILE PRO SER GLU ASN LEU PHE PHE GLY LEU ASP PRO TYR
SEQRES 12 B 555 LYS ARG TYR TYR PHE VAL HIS SER PHE ALA ALA ILE LEU
SEQRES 13 B 555 ASN SER GLU LYS LYS LYS ASN LEU GLU ASN ASP GLY TRP
SEQRES 14 B 555 LYS ILE ALA LYS ALA LYS TYR GLY SER GLU GLU PHE ILE
SEQRES 15 B 555 ALA ALA VAL ASN LYS ASN ASN ILE PHE ALA THR GLN PHE
SEQRES 16 B 555 HIS PRO GLU LYS SER GLY LYS ALA GLY LEU ASN VAL ILE
SEQRES 17 B 555 GLU ASN PHE LEU LYS GLN GLN SER PRO PRO ILE PRO ASN
SEQRES 18 B 555 TYR SER ALA GLU GLU LYS GLU LEU LEU MET ASN ASP TYR
SEQRES 19 B 555 SER ASN TYR GLY LEU THR ARG ARG ILE ILE ALA CYS LEU
SEQRES 20 B 555 ASP VAL ARG THR ASN ASP GLN GLY ASP LEU VAL VAL THR
SEQRES 21 B 555 LYS GLY ASP GLN TYR ASP VAL ARG GLU LYS SER ASP GLY
SEQRES 22 B 555 LYS GLY VAL ARG ASN LEU GLY LYS PRO VAL GLN LEU ALA
SEQRES 23 B 555 GLN LYS TYR TYR GLN GLN GLY ALA ASP GLU VAL THR PHE
SEQRES 24 B 555 LEU ASN ILE THR SER PHE ARG ASP CYS PRO LEU LYS ASP
SEQRES 25 B 555 THR PRO MET LEU GLU VAL LEU LYS GLN ALA ALA LYS THR
SEQRES 26 B 555 VAL PHE VAL PRO LEU THR VAL GLY GLY GLY ILE LYS ASP
SEQRES 27 B 555 ILE VAL ASP VAL ASP GLY THR LYS ILE PRO ALA LEU GLU
SEQRES 28 B 555 VAL ALA SER LEU TYR PHE ARG SER GLY ALA ASP LYS VAL
SEQRES 29 B 555 SER ILE GLY THR ASP ALA VAL TYR ALA ALA GLU LYS TYR
SEQRES 30 B 555 TYR GLU LEU GLY ASN ARG GLY ASP GLY THR SER PRO ILE
SEQRES 31 B 555 GLU THR ILE SER LYS ALA TYR GLY ALA GLN ALA VAL VAL
SEQRES 32 B 555 ILE SER VAL ASP PRO LYS ARG VAL TYR VAL ASN SER GLN
SEQRES 33 B 555 ALA ASP THR LYS ASN LYS VAL PHE GLU THR GLU TYR PRO
SEQRES 34 B 555 GLY PRO ASN GLY GLU LYS TYR CYS TRP TYR GLN CYS THR
SEQRES 35 B 555 ILE LYS GLY GLY ARG GLU SER ARG ASP LEU GLY VAL TRP
SEQRES 36 B 555 GLU LEU THR ARG ALA CYS GLU ALA LEU GLY ALA GLY GLU
SEQRES 37 B 555 ILE LEU LEU ASN CYS ILE ASP LYS ASP GLY SER ASN SER
SEQRES 38 B 555 GLY TYR ASP LEU GLU LEU ILE GLU HIS VAL LYS ASP ALA
SEQRES 39 B 555 VAL LYS ILE PRO VAL ILE ALA SER SER GLY ALA GLY VAL
SEQRES 40 B 555 PRO GLU HIS PHE GLU GLU ALA PHE LEU LYS THR ARG ALA
SEQRES 41 B 555 ASP ALA CYS LEU GLY ALA GLY MET PHE HIS ARG GLY GLU
SEQRES 42 B 555 PHE THR VAL ASN ASP VAL LYS GLU TYR LEU LEU GLU HIS
SEQRES 43 B 555 GLY LEU LYS VAL ARG MET ASP GLU GLU
HET NI A 902 1
HET SO4 A 801 5
HET SO4 A 802 5
HET SO4 A 806 5
HET NI B 901 1
HET SO4 B 803 5
HET SO4 B 804 5
HET POP B 999 9
HETNAM NI NICKEL (II) ION
HETNAM SO4 SULFATE ION
HETNAM POP PYROPHOSPHATE 2-
FORMUL 3 NI 2(NI 2+)
FORMUL 4 SO4 5(O4 S 2-)
FORMUL 10 POP H2 O7 P2 2-
FORMUL 11 HOH *281(H2 O)
HELIX 1 1 GLN A 15 HIS A 23 1 9
HELIX 2 2 PRO A 34 ASP A 36 5 3
HELIX 3 3 ILE A 39 GLY A 41 5 3
HELIX 4 4 TYR A 53 ASN A 62 1 10
HELIX 5 5 PHE A 65 SER A 75 1 11
HELIX 6 6 CYS A 83 LEU A 89 5 7
HELIX 7 7 VAL A 94 SER A 96 5 3
HELIX 8 8 SER A 155 ASN A 163 1 9
HELIX 9 9 PRO A 194 LYS A 196 5 3
HELIX 10 10 GLY A 198 LYS A 210 1 13
HELIX 11 11 ALA A 221 LEU A 227 1 7
HELIX 12 12 SER A 232 GLY A 235 5 4
HELIX 13 13 GLY A 277 GLN A 288 1 12
HELIX 14 14 LEU A 307 ASP A 309 5 3
HELIX 15 15 PRO A 311 LYS A 321 1 11
HELIX 16 16 ALA A 346 SER A 356 1 11
HELIX 17 17 THR A 365 GLU A 376 1 12
HELIX 18 18 PRO A 386 TYR A 394 1 9
HELIX 19 19 ALA A 396 ALA A 398 5 3
HELIX 20 20 GLN A 413 ASP A 415 5 3
HELIX 21 21 VAL A 451 LEU A 461 1 11
HELIX 22 22 LEU A 482 ALA A 491 1 10
HELIX 23 23 PRO A 505 LYS A 514 1 10
HELIX 24 24 GLY A 524 HIS A 527 1 4
HELIX 25 25 VAL A 533 HIS A 543 1 11
HELIX 26 26 GLN B 15 HIS B 23 1 9
HELIX 27 27 PRO B 34 ASP B 36 5 3
HELIX 28 28 ILE B 39 GLY B 41 5 3
HELIX 29 29 TYR B 53 ASN B 62 1 10
HELIX 30 30 PHE B 65 SER B 75 1 11
HELIX 31 31 CYS B 83 LEU B 89 5 7
HELIX 32 32 VAL B 94 SER B 96 5 3
HELIX 33 33 SER B 155 ASN B 163 1 9
HELIX 34 34 PRO B 194 LYS B 196 5 3
HELIX 35 35 GLY B 198 LEU B 209 1 12
HELIX 36 36 ALA B 221 LEU B 227 1 7
HELIX 37 37 SER B 232 GLY B 235 5 4
HELIX 38 38 GLY B 277 GLN B 288 1 12
HELIX 39 39 LEU B 307 ASP B 309 5 3
HELIX 40 40 PRO B 311 LYS B 321 1 11
HELIX 41 41 ALA B 346 SER B 356 1 11
HELIX 42 42 THR B 365 GLU B 376 1 12
HELIX 43 43 PRO B 386 TYR B 394 1 9
HELIX 44 44 ALA B 396 ALA B 398 5 3
HELIX 45 45 GLN B 413 ASP B 415 5 3
HELIX 46 46 VAL B 451 LEU B 461 1 11
HELIX 47 47 LEU B 482 ALA B 491 1 10
HELIX 48 48 PRO B 505 LYS B 514 1 10
HELIX 49 49 GLY B 524 HIS B 527 1 4
HELIX 50 50 VAL B 533 HIS B 543 1 11
SHEET 1 A 7 GLU A 27 VAL A 31 0
SHEET 2 A 7 VAL A 3 ILE A 7 1 N VAL A 4 O GLU A 27
SHEET 3 A 7 LEU A 45 GLY A 49 1 N ILE A 46 O HIS A 5
SHEET 4 A 7 ILE A 79 CYS A 83 1 N MET A 80 O LEU A 45
SHEET 5 A 7 ILE A 187 THR A 190 1 N PHE A 188 O ILE A 79
SHEET 6 A 7 GLU A 176 LYS A 184 -1 N LYS A 184 O ILE A 187
SHEET 7 A 7 LYS A 167 TYR A 173 -1 N TYR A 173 O GLU A 176
SHEET 1 B 2 GLU A 121 ASN A 125 0
SHEET 2 B 2 TYR A 143 HIS A 147 -1 N HIS A 147 O GLU A 121
SHEET 1 C 8 ALA A 519 GLY A 522 0
SHEET 2 C 8 ARG A 239 ARG A 247 1 N ARG A 239 O CYS A 520
SHEET 3 C 8 GLU A 293 ILE A 299 1 N GLU A 293 O ALA A 242
SHEET 4 C 8 PRO A 326 GLY A 330 1 N PRO A 326 O VAL A 294
SHEET 5 C 8 LYS A 360 ILE A 363 1 N LYS A 360 O VAL A 329
SHEET 6 C 8 VAL A 399 PRO A 405 1 N VAL A 400 O VAL A 361
SHEET 7 C 8 GLU A 465 CYS A 470 1 N GLU A 465 O ILE A 401
SHEET 8 C 8 PRO A 495 ALA A 498 1 N PRO A 495 O ILE A 466
SHEET 1 D 2 PRO A 405 VAL A 410 0
SHEET 2 D 2 TYR A 433 CYS A 438 -1 N GLN A 437 O LYS A 406
SHEET 1 E 7 VAL B 28 VAL B 31 0
SHEET 2 E 7 VAL B 4 ILE B 7 1 N VAL B 4 O GLN B 29
SHEET 3 E 7 LEU B 45 GLY B 49 1 N ILE B 46 O HIS B 5
SHEET 4 E 7 ILE B 79 CYS B 83 1 N MET B 80 O LEU B 45
SHEET 5 E 7 ILE B 187 THR B 190 1 N PHE B 188 O ILE B 79
SHEET 6 E 7 GLU B 176 LYS B 184 -1 N LYS B 184 O ILE B 187
SHEET 7 E 7 LYS B 167 TYR B 173 -1 N TYR B 173 O GLU B 176
SHEET 1 F 2 GLU B 121 ASN B 125 0
SHEET 2 F 2 TYR B 143 HIS B 147 -1 N HIS B 147 O GLU B 121
SHEET 1 G 8 CYS B 520 GLY B 522 0
SHEET 2 G 8 ILE B 240 VAL B 246 1 N ILE B 241 O CYS B 520
SHEET 3 G 8 GLU B 293 ASN B 298 1 N GLU B 293 O ALA B 242
SHEET 4 G 8 PRO B 326 GLY B 330 1 N PRO B 326 O VAL B 294
SHEET 5 G 8 LYS B 360 ILE B 363 1 N LYS B 360 O VAL B 329
SHEET 6 G 8 VAL B 399 PRO B 405 1 N VAL B 400 O VAL B 361
SHEET 7 G 8 GLU B 465 CYS B 470 1 N GLU B 465 O ILE B 401
SHEET 8 G 8 PRO B 495 ALA B 498 1 N PRO B 495 O ILE B 466
SHEET 1 H 2 PRO B 405 VAL B 410 0
SHEET 2 H 2 TYR B 433 CYS B 438 -1 N GLN B 437 O LYS B 406
LINK N GLY A -3 NI NI A 902 1555 1555 2.33
LINK N SER A -2 NI NI A 902 1555 1555 2.15
LINK ND1 HIS A -1 NI NI A 902 1555 1555 1.95
LINK N HIS A -1 NI NI A 902 1555 1555 2.00
LINK N GLY B -3 NI NI B 901 1555 1555 2.23
LINK N SER B -2 NI NI B 901 1555 1555 1.98
LINK ND1 HIS B -1 NI NI B 901 1555 1555 2.23
LINK N HIS B -1 NI NI B 901 1555 1555 2.02
CISPEP 1 VAL A 119 PRO A 120 0 0.73
CISPEP 2 VAL B 119 PRO B 120 0 0.63
SITE 1 AC1 4 GLY B -3 SER B -2 HIS B -1 MET B 1
SITE 1 AC2 5 HIS A -1 GLY A -3 SER A -2 MET A 1
SITE 2 AC2 5 TYR B 425
SITE 1 AC3 2 GLY A 364 THR A 365
SITE 1 AC4 5 GLY A 475 SER A 500 GLY A 501 HOH A 961
SITE 2 AC4 5 HOH A1034
SITE 1 AC5 3 LYS B 158 LYS B 170 LYS B 343
SITE 1 AC6 5 GLY B 331 GLY B 364 THR B 365 HOH B1107
SITE 2 AC6 5 HOH B1126
SITE 1 AC7 4 SER A 130 ASN A 132 HOH A1027 LYS B 493
SITE 1 AC8 11 ASP B 474 GLY B 475 ASN B 477 SER B 500
SITE 2 AC8 11 GLY B 501 GLY B 524 MET B 525 ARG B 528
SITE 3 AC8 11 HOH B1013 HOH B1050 HOH B1095
CRYST1 97.000 112.000 114.800 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010306 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008928 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008704 0.00000
MTRIX1 1 -0.843300 0.170100 -0.509800 128.05760 1
MTRIX2 1 0.104700 0.982400 0.154600 -62.61330 1
MTRIX3 1 0.527200 0.077000 -0.846300 -15.75990 1
(ATOM LINES ARE NOT SHOWN.)
END